6r0m
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==Histone fold domain of AtNF-YB2/NF-YC3 in P212121== |
- | <StructureSection load='6r0m' size='340' side='right'caption='[[6r0m]]' scene=''> | + | <StructureSection load='6r0m' size='340' side='right'caption='[[6r0m]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6r0m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R0M FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0m OCA], [https://pdbe.org/6r0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0m RCSB], [https://www.ebi.ac.uk/pdbsum/6r0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0m ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0m OCA], [https://pdbe.org/6r0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0m RCSB], [https://www.ebi.ac.uk/pdbsum/6r0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/NFYB2_ARATH NFYB2_ARATH] Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity).[UniProtKB:Q84W66] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | NF-Y transcription factor comprises three subunits: NF-YA, NF-YB and NF-YC. NF-YB and NF-YC dimerize through their histone fold domain (HFD), which can bind DNA in a non-sequence-specific fashion while serving as a scaffold for NF-YA trimerization. Upon trimerization, NF-YA specifically recognizes the CCAAT box sequence on promoters and enhancers. In plants, each NF-Y subunit is encoded by several genes giving rise to hundreds of potential heterotrimeric combinations. In addition, plant NF-YBs and NF-YCs interact with other protein partners to recognize a plethora of genomic motifs, as the CCT protein family that binds CORE sites. The NF-Y subunit organization and its DNA-binding properties, together with the NF-Y HFD capacity to adapt different protein modules, represent plant-specific features that play a key role in development, growth and reproduction. Despite their relevance, these features are still poorly understood at the molecular level. Here, we present the structures of Arabidopsis and rice NF-YB/NF-YC dimers, and of an Arabidopsis NF-Y trimer in complex with the FT CCAAT box, together with biochemical data on NF-Y mutants. The dimeric structures identify the key residues for NF-Y HFD stabilization. The NF-Y/DNA structure and the mutation experiments shed light on HFD trimerization interface properties and the NF-YA sequence appetite for the bases flanking the CCAAT motif. These data explain the logic of plant NF-Y gene expansion: the trimerization adaptability and the flexible DNA-binding rules serve the scopes of accommodating the large number of NF-YAs, CCTs and possibly other NF-Y HFD binding partners and a diverse audience of genomic motifs. | ||
+ | |||
+ | Structural determinants for NF-Y subunit organization and NF-Y/DNA association in plants.,Chaves-Sanjuan A, Gnesutta N, Gobbini A, Martignago D, Bernardini A, Fornara F, Mantovani R, Nardini M Plant J. 2021 Jan;105(1):49-61. doi: 10.1111/tpj.15038. Epub 2020 Nov 27. PMID:33098724<ref>PMID:33098724</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6r0m" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Nuclear transcription factor Y|Nuclear transcription factor Y]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Bernardini A]] |
+ | [[Category: Chaves-Sanjuan A]] | ||
+ | [[Category: Chiara M]] | ||
+ | [[Category: Fornara F]] | ||
+ | [[Category: Gnesutta N]] | ||
+ | [[Category: Horner D]] | ||
+ | [[Category: Mantovani R]] | ||
+ | [[Category: Nardini M]] |
Current revision
Histone fold domain of AtNF-YB2/NF-YC3 in P212121
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